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P32327 (PYC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate carboxylase 2

EC=6.4.1.1
Alternative name(s):
Pyruvic carboxylase 2
Short name=PCB 2
Gene names
Name:PYC2
Ordered Locus Names:YBR218C
ORF Names:YBR1507
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

Catalytic activity

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactor

Biotin.

Zinc.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Induction

By glucose.

Miscellaneous

Present with 17000 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 11801179Pyruvate carboxylase 2
PRO_0000146825

Regions

Domain19 – 471453Biotin carboxylation
Domain141 – 338198ATP-grasp
Domain558 – 825268Carboxyltransferase
Domain1102 – 116968Biotinyl-binding
Region566 – 5705Substrate binding By similarity

Sites

Active site3131 By similarity
Metal binding5671Divalent metal cation By similarity
Metal binding7351Divalent metal cation; via carbamate group By similarity
Metal binding7651Divalent metal cation By similarity
Metal binding7671Divalent metal cation By similarity
Binding site1371ATP By similarity
Binding site2211ATP By similarity
Binding site2561ATP By similarity
Binding site6391Substrate By similarity
Binding site8991Substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue7351N6-carboxylysine By similarity
Modified residue11361N6-biotinyllysine By similarity

Experimental info

Sequence conflict151S → C in CAA42544. Ref.1
Sequence conflict1321D → E in CAA42544. Ref.1
Sequence conflict2381N → K in CAA42544. Ref.1
Sequence conflict2681L → F in CAA42544. Ref.1
Sequence conflict5461S → C in CAA42544. Ref.1
Sequence conflict6421N → T in CAA42544. Ref.1
Sequence conflict771 – 7733GTA → STR in CAA42544. Ref.1
Sequence conflict8311W → R in CAA42544. Ref.1
Sequence conflict8391S → P in CAA42544. Ref.1
Sequence conflict10011Y → N in CAA42544. Ref.1
Sequence conflict11551K → R in CAA42544. Ref.1
Sequence conflict11781Q → P in CAA42544. Ref.1
Sequence conflict11801K → KVIFTR in CAA42544. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32327 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: AD60DA3A60F5E001

FASTA1,180130,167
        10         20         30         40         50         60 
MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY SHEDRLSMHR 

        70         80         90        100        110        120 
LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH PGYGFLSENS EFADKVVKAG 

       130        140        150        160        170        180 
ITWIGPPAEV IDSVGDKVSA RHLAARANVP TVPGTPGPIE TVQEALDFVN EYGYPVIIKA 

       190        200        210        220        230        240 
AFGGGGRGMR VVREGDDVAD AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG 

       250        260        270        280        290        300 
NVVHLFERDC SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD 

       310        320        330        340        350        360 
NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD KITTRGFSIQ 

       370        380        390        400        410        420 
CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG ATISPHYDSM LVKCSCSGST 

       430        440        450        460        470        480 
YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN 

       490        500        510        520        530        540 
RAQKLLHYLA DLAVNGSSIK GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL 

       550        560        570        580        590        600 
LEKGPSEFAK QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE 

       610        620        630        640        650        660 
CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP DNAIDHFVKQ 

       670        680        690        700        710        720 
AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC YSGDMLQPGK KYNLDYYLEV 

       730        740        750        760        770        780 
VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI GSLRTRYPDL PIHVHSHDSA GTAVASMTAC 

       790        800        810        820        830        840 
ALAGADVVDV AINSMSGLTS QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC 

       850        860        870        880        890        900 
FEADLKGPDP EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP 

       910        920        930        940        950        960 
TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF PEPLRSDVLR 

       970        980        990       1000       1010       1020 
NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS YNMYPRVYED FQKIRETYGD 

      1030       1040       1050       1060       1070       1080 
LSVLPTKNFL APAEPDEEIE VTIEQGKTLI IKLQAVGDLN KKTGQREVYF ELNGELRKIR 

      1090       1100       1110       1120       1130       1140 
VADKSQNIQS VAKPKADVHD THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV 

      1150       1160       1170       1180 
VSSPADGQVK DVFIKDGESV DASDLLVVLE EETLPPSQKK 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains."
Stucka R., Dequin S., Salmon J.-M., Gancedo C.
Mol. Gen. Genet. 229:307-315(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects on protein biotinylation."
Val D.L., Chapman-Smith A., Walker M.E., Cronan J.E. Jr., Wallace J.C.
Biochem. J. 312:817-825(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59890 Genomic DNA. Translation: CAA42544.1.
U35647 Genomic DNA. Translation: AAC49147.1.
Z36087 Genomic DNA. Translation: CAA85182.1.
BK006936 Genomic DNA. Translation: DAA07334.1.
PIRS46094.
RefSeqNP_009777.1. NM_001178566.1.

3D structure databases

ProteinModelPortalP32327.
SMRP32327. Positions 22-1170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32915. 86 interactions.
DIPDIP-6426N.
IntActP32327. 2 interactions.
MINTMINT-2781496.
STRING4932.YBR218C.

Proteomic databases

PaxDbP32327.
PeptideAtlasP32327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR218C; YBR218C; YBR218C.
GeneID852519.
KEGGsce:YBR218C.

Organism-specific databases

CYGDYBR218c.
SGDS000000422. PYC2.

Phylogenomic databases

eggNOGCOG1038.
GeneTreeENSGT00750000118625.
HOGENOMHOG000282801.
KOK01958.
OMALDYYLEV.
OrthoDBEOG7GQZ41.

Enzyme and pathway databases

BioCycYEAST:YBR218C-MONOMER.
BRENDA6.4.1.1. 984.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP32327.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR18866:SF10. PTHR18866:SF10. 1 hit.
PfamPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFPIRSF001594. Pyruv_carbox. 1 hit.
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01235. pyruv_carbox. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971553.

Entry information

Entry namePYC2_YEAST
AccessionPrimary (citable) accession number: P32327
Secondary accession number(s): D6VQL4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways